Artificial coiled coil biomineralisation protein for the synthesis of magnetic nanoparticles

Andrea E. Rawlings, Lori A. Somner, Michaela Fitzpatrick-Milton, Thomas P. Roebuck, Christopher Gwyn, Panah Liravi, Victoria Seville, Thomas J. Neal, Oleksandr O. Mykhaylyk, Stephen A. Baldwin and Sarah S. Staniland ()
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Andrea E. Rawlings: University of Sheffield
Lori A. Somner: University of Sheffield
Michaela Fitzpatrick-Milton: University of Sheffield
Thomas P. Roebuck: University of Leeds
Christopher Gwyn: University of Leeds
Panah Liravi: University of Leeds
Victoria Seville: University of Sheffield
Thomas J. Neal: University of Sheffield
Oleksandr O. Mykhaylyk: University of Sheffield
Stephen A. Baldwin: University of Leeds
Sarah S. Staniland: University of Sheffield

Nature Communications, 2019, vol. 10, issue 1, 1-9

Abstract: Abstract Green synthesis of precise inorganic nanomaterials is a major challenge. Magnetotactic bacteria biomineralise magnetite nanoparticles (MNPs) within membrane vesicles (magnetosomes), which are embedded with dedicated proteins that control nanocrystal formation. Some such proteins are used in vitro to control MNP formation in green synthesis; however, these membrane proteins self-aggregate, making their production and use in vitro challenging and difficult to scale. Here, we provide an alternative solution by displaying active loops from biomineralisation proteins Mms13 and MmsF on stem-loop coiled-coil scaffold proteins (Mms13cc/MmsFcc). These artificial biomineralisation proteins form soluble, stable alpha-helical hairpin monomers, and MmsFcc successfully controls the formation of MNP when added to magnetite synthesis, regulating synthesis comparably to native MmsF. This study demonstrates how displaying active loops from membrane proteins on coiled-coil scaffolds removes membrane protein solubility issues, while retains activity, enabling a generic approach to readily-expressible, versatile, artificial membrane proteins for more accessible study and exploitation.

Date: 2019
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DOI: 10.1038/s41467-019-10578-2

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